ID ALG11_EREGS Reviewed; 582 AA. AC Q75B12; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 106. DE RecName: Full=GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase; DE EC=2.4.1.131; DE AltName: Full=Alpha-1,2-mannosyltransferase ALG11; DE AltName: Full=Asparagine-linked glycosylation protein 11; DE AltName: Full=Glycolipid 2-alpha-mannosyltransferase; GN Name=ALG11; OrderedLocusNames=ADL235W; OS Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL OS Y-1056) (Yeast) (Ashbya gossypii). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Eremothecium. OX NCBI_TaxID=284811; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=15001715; DOI=10.1126/science.1095781; RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., RA Gaffney T.D., Philippsen P.; RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces RT cerevisiae genome."; RL Science 304:304-307(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056; RX PubMed=23749448; DOI=10.1534/g3.112.002881; RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.; RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type RT loci, numerous translocations, lack of transposons, and distinct gene RT duplications."; RL G3 (Bethesda) 3:1225-1239(2013). CC -!- FUNCTION: Required for N-linked oligosaccharide assembly. Has a role in CC the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core CC oligosaccharide on the cytoplasmic face of the endoplasmic reticulum CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)- CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha- CC D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)- CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D- CC GlcNAc-diphosphodolichol + 2 GDP + 2 H(+); Xref=Rhea:RHEA:29523, CC Rhea:RHEA-COMP:12626, Rhea:RHEA-COMP:12627, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57527, ChEBI:CHEBI:58189, ChEBI:CHEBI:132511, CC ChEBI:CHEBI:132515; EC=2.4.1.131; CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; CC Single-pass type II membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016817; AAS51685.1; -; Genomic_DNA. DR RefSeq; NP_983861.1; NM_209214.1. DR AlphaFoldDB; Q75B12; -. DR STRING; 284811.Q75B12; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR GlyCosmos; Q75B12; 3 sites, No reported glycans. DR EnsemblFungi; AAS51685; AAS51685; AGOS_ADL235W. DR GeneID; 4619996; -. DR KEGG; ago:AGOS_ADL235W; -. DR eggNOG; KOG1387; Eukaryota. DR HOGENOM; CLU_017896_1_1_1; -. DR InParanoid; Q75B12; -. DR OMA; WKHFTLI; -. DR OrthoDB; 197751at2759; -. DR UniPathway; UPA00378; -. DR Proteomes; UP000000591; Chromosome IV. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0004377; F:GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; IEA:EnsemblFungi. DR GO; GO:0006490; P:oligosaccharide-lipid intermediate biosynthetic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR CDD; cd03806; GT4_ALG11-like; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1. DR InterPro; IPR038013; ALG11. DR InterPro; IPR031814; ALG11_N. DR InterPro; IPR001296; Glyco_trans_1. DR PANTHER; PTHR45919; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1. DR PANTHER; PTHR45919:SF1; GDP-MAN:MAN(3)GLCNAC(2)-PP-DOL ALPHA-1,2-MANNOSYLTRANSFERASE; 1. DR Pfam; PF15924; ALG11_N; 1. DR Pfam; PF00534; Glycos_transf_1; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. PE 3: Inferred from homology; KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; KW Reference proteome; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..582 FT /note="GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2- FT mannosyltransferase" FT /id="PRO_0000080272" FT TOPO_DOM 1..12 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 13..33 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 34..582 FT /note="Lumenal" FT /evidence="ECO:0000255" FT CARBOHYD 314 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 331 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 499 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 582 AA; 66635 MW; BE8C12857524068E CRC64; MESCWLTMES YQAALVVCIV SGLILAVAGY GNVRRLACEF LLKPPKRFRD DICEALLRGP ENDQKPVLVD FGWRHGAVRR QMLLASAKAS AYSNERHGSK IHISPDDIAR GRSFADALDV HRRSGRILFG FFHPFCNAGG GGEKVLWKAV ETTLKQSLNN IVVVYTGDCD TTGARILSNV EHRFGSQLDS ERIVFIFLRH RKWVESRTWP RMTLLGQALG SIVLSIEAAL CCPPDVWCDT MGYPFGYPFV SWLCRIPIIT YTHYPVVSID MLDKLRMMPE FRNSPTLWAK FLYWRIFMRC YTFAGSFVDL AVTNSTWTYN HINAIWSRTG NVSIIYPPCS TENLVIENAH DMWDRKHQAV VIAQFRPEKR HALILRSFSN FVKKTGSNMK LLMLGSTRGQ EDRDYVKKLE QLAYSELAIP KESLEFITDC KYEKMKKYLQ ESSFGINAMW NEHFGIAVVE YAASGLITLA HASAGPLLDI IVPWDIEGDK QLERGSDKNR TGFFFKDRSD PDFCKITAEF PTLEELFVRA DQLTDEERLA ISQRAKRCVL HKFSDLKFSE DWAQVVDRTI QLLHTLRNDK VE //